title: Morphological characterization of the erythrocyte membrane related to myxovirus receptors.
abstract: The receptor of myxoviral hemagglutinins is defined by terminal sialic acid residues of the major sialoglycoprotein (glycophorin) of the human erythrocyte membrane. A number of lectins and antibodies are suitable to specifically label this molecule. The proposed association of glycophorin with the structures revealed as intramembrane particles (IMP) on freeze-fractured membranes rests only on indirect evidence; IMP are not composed of glycophorin alone but glycophorin may be a component of them in association with other integral membrane proteins and/or lipids. Mapping experiments employing limulin, a lectin specific for sialic acids, and anti-glycophorin are described. These experiments demonstrate a lack of association of glycophorin and the IMP.
mesh_terms: D004910:Erythrocyte Membrane / Q000032:analysis / Q000648:ultrastructure*; D004912:Erythrocytes / Q000648:ultrastructure*; D005614:Freeze Fracturing; D006021:Glycophorins / Q000032:analysis*; D006801:Humans; D007118:Immunoassay; D037102:Lectins; D008854:Microscopy, Electron; D009975:Orthomyxoviridae; D011991:Receptors, Virus / Q000032:analysis*; D012795:Sialoglycoproteins / Q000032:analysis*
chemical_list: D006021:Glycophorins; D037102:Lectins; D011991:Receptors, Virus; D012795:Sialoglycoproteins; C015323:limulin